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CATH domain | Related DB codes (homologues) |
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3.40.50.1820 : Rossmann fold | S00544,S00344,S00517,S00525,S00526,S00720,S00723,S00724,S00725,S00919,S00057,S00374,S00345,S00347,S00348,S00346,S00350,S00352,S00353,S00356,S00358,D00189,D00210,D00539,T00253 |
Enzyme Name | UniProtKB | KEGG |
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| O05149 | Q84II3 |
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Protein name |
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| 2,6-dioxo-6-phenylhexa-3-enoate hydrolaseHOHPDA hydrolase |
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Synonyms | 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase | Meta cleavage compound hydrolase |
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KEGG pathways | MAP code | Pathways |
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MAP00621 | Biphenyl degradation | MAP00628 | Fluorene degradation |
UniProtKB:Accession Number | O05149 | Q84II3 |
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Entry name | O05149_RHOSO | Q84II3_9BURK |
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Activity |
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Subunit |
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Subcellular location |
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Cofactor |
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Compound table: links to PDB-related databases & PoSSuM |
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| Substrates | Products |
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KEGG-id | C01273 | C00001 | C00180 | C00596 |
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Compound | 2,6-Dioxo-6-phenylhexa-3-enoate | H2O | Benzoate | 2-Oxopent-4-enoate |
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Type | aromatic ring (only carbon atom),carbohydrate,carboxyl group | H2O | aromatic ring (only carbon atom),carboxyl group | carbohydrate,carboxyl group |
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ChEBI |
| 15377
| 30746
| 1113
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PubChem |
| 962 22247451
| 243 20144841
| 5280361
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1c4xA |  |  |  |  |  |  |  | Unbound | | Unbound | Unbound |
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1j1iA |  |  |  |  |  |  |  | Unbound | | Unbound | Unbound |
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References for Catalytic Mechanism | References | Sections | No. of steps in catalysis |
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[2] | p.1144-1146 |
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references | [1] |
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Journal | Proc Jpn Acad Ser B |
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Year | 1997 |
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Volume | 73 |
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Pages | 154-7 |
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Authors | N.Nandhagopal, T.Senda, T.Hatta, A.Yamada, E.Masai, M.Fukuda, Y.Mitsui |
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Title | Three-dimensional structure of microbial 2-hydroxyl-6-oxo-6-phenylhexa-2,4- dienoic acid (hpda) hydrolase (bphd enzyme) from rhodococcussp. Strain rha1, in the pcb degradation pathway. |
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Related PDB | 1c4x |
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[2] |
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Comments | X-ray crystallography (2.4 Angstroms) |
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PubMed ID | 11399084 |
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Journal | J Mol Biol |
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Year | 2001 |
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Volume | 309 |
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Pages | 1139-51 |
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Authors | Nandhagopal N, Yamada A, Hatta T, Masai E, Fukuda M, Mitsui Y, Senda T |
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Title | Crystal structure of 2-hydroxyl-6-oxo-6-phenylhexa-2,4-dienoic acid (HPDA) hydrolase (BphD enzyme) from the Rhodococcus sp. strain RHA1 of the PCB degradation pathway. |
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Related PDB | 1c4x |
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[3] |
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PubMed ID | 12659866 |
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Journal | Biochem Biophys Res Commun |
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Year | 2003 |
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Volume | 303 |
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Pages | 631-9 |
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Authors | Habe H, Morii K, Fushinobu S, Nam JW, Ayabe Y, Yoshida T, Wakagi T, Yamane H, Nojiri H, Omori T |
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Title | Crystal structure of a histidine-tagged serine hydrolase involved in the carbazole degradation (CarC enzyme). |
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Related PDB | 1j1i |
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comments | The paper [2] mentioned that, although the catalytic mechanism of this enzyme might be similar to that of other alpha/beta-hydrolases, there is a significant differences between them. The literature mentioned that a chemical modification to the possible nucleophile, Ser110, might play a role in the catalytic mechanism, which can be required to hydrolyze carbon-carbon bonds [2]. Although the literature [2] mentioned that His35/Gly36 (of 1c4x) might form an oxyanion hole, these residues are a bit far from the active site. Instead, comparison with other homologus enzymes (T00253, S00345, S00347, S00350, S00374), which have got Ser/His/Asp as catalytic triad with complex structure determined, suggested that mainchain amide groups of Ala37 and Met111 must form an oxyanion hole. On the other hand, recent study on the homologous enzyme, which also catalyzes hydrolysis of Ketonic carbon-carbon bond suggested totally different mechanism, which involves isomerization (S00526 in EzCatDB).
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created | updated |
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2002-07-04 | 2009-03-30 |
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